about
Remodeling of channel-forming ORAI proteins determines an oncogenic switch in prostate cancerTRP channel-associated factors are a novel protein family that regulates TRPM8 trafficking and activity.Caveolae contribute to the apoptosis resistance induced by the alpha(1A)-adrenoceptor in androgen-independent prostate cancer cellsThe transient receptor potential channel TRPM8 is inhibited via the alpha 2A adrenoreceptor signaling pathwayORAI1 calcium channel orchestrates skin homeostasis.Effects of hyperprolactinemia on rat prostate growth: evidence of androgeno-dependence.Overexpression of an alpha 1H (Cav3.2) T-type calcium channel during neuroendocrine differentiation of human prostate cancer cells.A new human gene KCNRG encoding potassium channel regulating protein is a cancer suppressor gene candidate located in 13q14.3.TRPV6 calcium channel translocates to the plasma membrane via Orai1-mediated mechanism and controls cancer cell survivalCytoskeleton reorganization as an alternative mechanism of store-operated calcium entry control in neuroendocrine-differentiated cells.Ion channels in the regulation of apoptosis.Orai1 contributes to the establishment of an apoptosis-resistant phenotype in prostate cancer cells.Voltage- and cold-dependent gating of single TRPM8 ion channels.Complex regulation of the TRPM8 cold receptor channel: role of arachidonic acid release following M3 muscarinic receptor stimulationTRPV2 mediates adrenomedullin stimulation of prostate and urothelial cancer cell adhesion, migration and invasion.Alpha1-adrenergic receptors activate Ca(2+)-permeable cationic channels in prostate cancer epithelial cells.Differential sensitivity of prostate tumor derived endothelial cells to sorafenib and sunitinib.Epidermal TRPM8 channel isoform controls the balance between keratinocyte proliferation and differentiation in a cold-dependent manner.Targeting of short TRPM8 isoforms induces 4TM-TRPM8-dependent apoptosis in prostate cancer cells.Cold/menthol TRPM8 receptors initiate the cold-shock response and protect germ cells from cold-shock-induced oxidationEarly effects of PRL on ion conductances in CHO cells expressing PRL receptor.Role of tyrosine phosphorylation in potassium channel activation. Functional association with prolactin receptor and JAK2 tyrosine kinase.Ion channels in death and differentiation of prostate cancer cells.Disrupting the dynamic equilibrium of ORAI channels determines the phenotype of malignant cellsCalcium signalling and cancer cell growth.Insights into Ca2+ homeostasis of advanced prostate cancer cells.TRPA1-dependent regulation of bladder detrusor smooth muscle contractility in normal and type I diabetic rats.Remodelling of Ca2+ transport in cancer: how it contributes to cancer hallmarks?The trans-membrane domain of Bcl-2α, but not its hydrophobic cleft, is a critical determinant for efficient IP3 receptor inhibition.Calcium in tumour metastasis: new roles for known actors.Ion channnels and transporters in cancer. 5. Ion channels in control of cancer and cell apoptosis.From urgency to frequency: facts and controversies of TRPs in the lower urinary tract.The role of the TRPV6 channel in cancer.Targeting Ca²⁺ transport in cancer: close reality or long perspective?Targeting apoptosis by the remodelling of calcium-transporting proteins in cancerogenesis.Calcium-permeable ion channels in control of autophagy and cancerCalcium homeostasis in cancer: A focus on senescence.Functional and physiopathological implications of TRP channels.The calcium-signaling toolkit: Updates needed.Human transient receptor potential (TRP) channel expression profiling in carcinogenesis.
P50
Q24299726-8FB88C7F-903D-4406-AB9F-6C054DF04327Q24312097-1BF2AAF8-C34E-4A58-AB52-3C670B008765Q28476183-D06F4FAE-36A5-4986-85EA-D4A10EA4FB6BQ28578194-6ADC198A-D752-4CC5-B113-ADFDA16ACC8BQ30559546-53B01E36-61E7-4AFE-8267-5DACD4036546Q31712792-47869D7B-E333-4101-94D5-6BD44EA9788BQ34110103-645D9FAD-1D5F-46C1-B956-0F9B4CD666B0Q34185354-2BC0A518-A65A-4133-9794-934F08589F52Q34218298-627492C6-D7F4-4437-B609-EE2AB6EA7C62Q34438254-DC6E89E2-F12E-4FF8-9B7D-93F9387C357AQ34450888-29A2260B-8386-40DD-862B-CD189DBE2DEFQ34545497-864BFC2E-F140-4CA9-8879-098F85980F7DQ34545661-F43B8186-20FB-4023-ACF4-CD3978398269Q34685475-22151459-0353-46FB-8E77-D847B9801451Q34760935-FCC38A7E-2E35-4CEC-B1A8-F2D2EEC9174CQ35019287-725B6F06-C606-4911-A8FA-8214EBB2D5C9Q35508739-0762F42D-21AD-4C49-ABF8-48697604599DQ35665134-FBFAF8F2-0A86-445E-A024-1F066010B8C0Q35988679-16306233-1A67-4500-8356-0C612FF0B4B1Q36056030-DAF4F256-1567-40C6-A6F7-48A7BD6FABC3Q36675845-48D9DE34-3CD3-43AE-B79D-982783D5F8F9Q36685326-43A32500-A27F-44A6-9067-67F417DC96D3Q36811138-2F567C05-C0FD-4B11-AA1D-C53667BE9FB6Q36997514-FE33D091-DFE6-418B-B287-8CC1106BAC46Q37056451-05BC1821-C050-4F54-B04E-D5A3A62634D6Q37429293-15F794CA-801D-4D35-ABEA-78355E709D2BQ37472557-BDDC9111-05C6-4122-A9D8-29BD75EE4694Q37566460-399B439C-2407-47A0-A5A9-AD9FD828D3E6Q37688303-5995E89D-596B-4F85-9E6C-481787FA107BQ37903657-C63BCBD4-7FD4-4790-8B2F-93F6488C51A3Q37937313-83D38C6D-538C-4BAE-81FF-62E81605C290Q37942411-F60FCB26-6F42-4782-BAB4-DCFD1052B33AQ37983769-535A757A-C5DC-47D5-931D-645B54324C1FQ38072110-43E97BC1-97FD-433C-B854-626695A3D76CQ38089963-2073335F-B8C7-4334-9588-475D14D05B44Q38150840-EA6EAE6F-5E2E-4A08-B874-29E898FF248FQ38375624-D12D38C5-9578-4545-B839-16DA88855F75Q38456330-61DBA27B-0D43-4533-9AFD-5EDCC110C478Q38666905-A66C3DB8-7153-41B6-A92E-2C212D3397B3Q38672715-F44FAB15-6D00-4247-8B5F-497E67FDC8FB
P50
description
researcher
@en
wetenschapper
@nl
name
Natacha B. Prevarskaya
@en
Prevarskaya NB
@ast
Prevarskaya NB
@nl
type
label
Natacha B. Prevarskaya
@en
Prevarskaya NB
@ast
Prevarskaya NB
@nl
altLabel
Prevarskaya NB
@en
prefLabel
Natacha B. Prevarskaya
@en
Prevarskaya NB
@ast
Prevarskaya NB
@nl
P106
P31
P496
0000-0003-0316-197X